Loss of core fucosylation in both ST6GAL1 and its substrate enhances glycoprotein sialylation in mice
| Autor: | Wenzhe Li, Weijie Dong, Akihiko Kameyama, Guoling Huang, Jianguo Gu, Gang Liu, Zhi Li, Shijie Sun, Yuqing Li |
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| Rok vydání: | 2020 |
| Předmět: |
Adult
Glycosylation Fucosyltransferase Biochemistry Mice 03 medical and health sciences 0302 clinical medicine Antigens CD Glycosyltransferase Animals Humans Molecular Biology Cells Cultured Fucosylation Aged Fucose Glycoproteins 030304 developmental biology Aged 80 and over Mice Knockout chemistry.chemical_classification 0303 health sciences Messenger RNA biology Substrate (chemistry) Cell Biology Middle Aged Fucosyltransferases Molecular biology Sialyltransferases Enzyme assay carbohydrates (lipids) Enzyme chemistry 030220 oncology & carcinogenesis biology.protein Female Glycoprotein |
| Zdroj: | Biochemical Journal. 477:1179-1201 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bcj20190789 |
| Popis: | Fucosyltransferase 8 (FUT8) and β-galactoside α-2,6-sialyltransferase 1 (ST6GAL1) are glycosyltransferases that catalyze α1,6-fucosylation and α2,6-sialylation, respectively, in the mammalian N-glycosylation pathway. They are aberrantly expressed in various human diseases. FUT8 is non-glycosylated but is responsible for the fucosylation of ST6GAL1. However, the mechanism for the interaction between these two enzymes is unknown. In this study, we show that serum levels of α2,6-sialylated N-glycans are increased in Fut8−/− mice, whereas the mRNA and protein levels of ST6GAL1 are unchanged in mouse live tissues. The level of α2,6-sialylation on IgG was also enhanced in Fut8−/− mice along with ST6GAL1 catalytic activity increase in both serum and liver. Moreover, it was observed that ST6GAL1 prefers non-fucosylated substrates. Interestingly, increased core fucosylation accompanied by a reduction in α2,6-sialylation, was detected in rheumatoid arthritis patient serum. These findings provide new insight into the interactions between FUT8 and ST6GAL1. |
| Databáze: | OpenAIRE |
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